1.
Nobel Prize in Physiology or Medicine
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The Nobel Prize in Physiology or Medicine, administered by the Nobel Foundation, is awarded once a year for outstanding discoveries in the fields of life sciences and medicine. It is one of five Nobel Prizes established in 1895 by Swedish chemist Alfred Nobel, Nobel was personally interested in experimental physiology and wanted to establish a prize for progress through scientific discoveries in laboratories. The Nobel Prize is presented to the recipient at a ceremony on 10 December, the anniversary of Nobels death, along with a diploma. The front side of the medal provides the profile of Alfred Nobel as depicted on the medals for Physics, Chemistry. As of 2015,106 Nobel Prizes in Physiology or Medicine have been awarded to 198 men and 12 women. The first Nobel Prize in Physiology or Medicine was awarded in 1901 to the German physiologist Emil von Behring, for his work on serum therapy and this includes one to António Egas Moniz in 1949 for the prefrontal leucotomy, bestowed despite protests from the medical establishment. Other controversies resulted from disagreements over who was included in the award, the 1952 prize to Selman Waksman was litigated in court, and half the patent rights awarded to his co-discoverer Albert Schatz who was not recognized by the prize. The 1962 prize awarded to James D, since the Nobel Prize rules forbid nominations of the deceased, longevity is an asset, one prize being awarded as long as 50 years after the discovery. Alfred Nobel was born on 21 October 1833 in Stockholm, Sweden into a family of engineers and he was a chemist, engineer and inventor who amassed a fortune during his lifetime, most of it from his 355 inventions of which dynamite is the most famous. He was interested in experimental physiology and set up his own labs in France, in 1888, Nobel was surprised to read his own obituary, titled The merchant of death is dead, in a French newspaper. Though Nobel wrote several wills during his lifetime, the last was written a little over a year before he died at the age of 63, because his will was contested, it was not approved by the Storting until 26 April 1897. After Nobels death, the Nobel Foundation was set up to manage the assets of the bequest, in 1900, the Nobel Foundations newly created statutes were promulgated by Swedish King Oscar II. According to Nobels will, the Karolinska Institutet in Sweden, a medical school, today, the prize is commonly referred to as the Nobel Prize in Medicine. It was important to Nobel that the prize be awarded for a discovery, per the provisions of the will, only select persons are eligible to nominate individuals for the award. Past Nobel laureates may also nominate, until 1977, all professors of Karolinska Institutet together decided on the Nobel Prize in Physiology or Medicine. Therefore, the Nobel Assembly was constituted, consisting of 50 professors at Karolinska Institutet. It elects the Nobel Committee with 5 members who evaluate the nominees, the Secretary who is in charge of the organization, in 1968, a provision was added that no more than three persons may share a Nobel prize. True to its mandate, the Committee has selected researchers working in the sciences over those who have made applied contributions
2.
Glycerol
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Glycerol /ˈɡlɪsərɒl/ is a simple polyol compound. It is a colorless, odorless, viscous liquid that is sweet-tasting, the glycerol backbone is found in all lipids known as triglycerides. It is widely used in the industry as a sweetener and humectant. Glycerol has three groups that are responsible for its solubility in water and its hygroscopic nature. Although achiral, glycerol is prochiral with respect to reactions of one of the two primary alcohols, thus, in substituted derivatives, the stereospecific numbering labels each carbon as either sn-1, sn-2, or sn-3. Glycerol is generally obtained from plant and animal sources where it occurs as triglycerides, triglycerides are esters of glycerol with long-chain carboxylic acids. Approximately 950,000 tons per year are produced in the United States and it was projected in 2006 that by the year 2020, production would be six times more than demand. Glycerol from triglycerides is produced on a scale, but the crude product is of variable quality. It can be purified, but the process is expensive, some glycerol is burned for energy, but its heat value is low. High purity glycerol is obtained by distillation, vacuum is helpful due to the high boiling point of glycerol. Although usually not cost-effective, glycerol can be produced by various routes from propylene and this epichlorohydrin is then hydrolyzed to give glycerol. Chlorine-free processes from propylene include the synthesis of glycerol from acrolein, because of the large-scale production of biodiesel from fats, where glycerol is a waste product, the market for glycerol is depressed. Thus, synthetic processes are not economical, owing to oversupply, efforts are being made to convert glycerol to synthetic precursors, such as acrolein and epichlorohydrin. In food and beverages, glycerol serves as a humectant, solvent, and sweetener and it is also used as filler in commercially prepared low-fat foods, and as a thickening agent in liqueurs. Glycerol and water are used to preserve certain types of plant leaves, as a sugar substitute, it has approximately 27 kilocalories per teaspoon and is 60% as sweet as sucrose. It does not feed the bacteria that form plaques and cause dental cavities, as a food additive, glycerol is labeled as E number E422. It is added to icing to prevent it from setting too hard, as used in foods, glycerol is categorized by the Academy of Nutrition and Dietetics as a carbohydrate. The U. S. Food and Drug Administration carbohydrate designation includes all caloric macronutrients excluding protein, glycerol is used in medical, pharmaceutical and personal care preparations, mainly as a means of improving smoothness, providing lubrication, and as a humectant
3.
Glycolysis
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Glycolysis is the metabolic pathway that converts glucose C6H12O6, into pyruvate, CH3COCOO− + H+. The free energy released in this process is used to form the high-energy molecules ATP, glycolysis is a determined sequence of ten enzyme-catalyzed reactions. The intermediates provide entry points to glycolysis, for example, most monosaccharides, such as fructose and galactose, can be converted to one of these intermediates. The intermediates may also be directly useful, for example, the intermediate dihydroxyacetone phosphate is a source of the glycerol that combines with fatty acids to form fat. Glycolysis is an oxygen independent metabolic pathway, meaning that it not use molecular oxygen for any of its reactions. However the products of glycolysis are sometimes metabolized using atmospheric oxygen, when molecular oxygen is used for the metabolism of the products of glycolysis the process is usually referred to as aerobic, whereas if no oxygen is used the process is said to be anaerobic. Thus, glycolysis occurs, with variations, in all organisms. The wide occurrence of glycolysis indicates that it is one of the most ancient metabolic pathways, glycolysis could thus have originated from chemical constraints of the prebiotic world. Glycolysis occurs in most organisms in the cytosol of the cell, the most common type of glycolysis is the Embden–Meyerhof–Parnas, which was discovered by Gustav Embden, Otto Meyerhof, and Jakub Karol Parnas. Glycolysis also refers to other pathways, such as the Entner–Doudoroff pathway, however, the discussion here will be limited to the Embden–Meyerhof–Parnas pathway. The overall reaction of glycolysis is, The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. In the cellular environment, all three groups of ADP dissociate into −O− and H+, giving ADP3−, and this ion tends to exist in an ionic bond with Mg2+. ATP behaves identically except that it has four groups, giving ATPMg2−. When these differences along with the charges on the two phosphate groups are considered together, the net charges of −4 on each side are balanced. For simple fermentations, the metabolism of one molecule of glucose to two molecules of pyruvate has a net yield of two molecules of ATP, most cells will then carry out further reactions to repay the used NAD+ and produce a final product of ethanol or lactic acid. Many bacteria use inorganic compounds as hydrogen acceptors to regenerate the NAD+, cells performing aerobic respiration synthesize much more ATP, but not as part of glycolysis. These further aerobic reactions use pyruvate and NADH + H+ from glycolysis, the pathway of glycolysis as it is known today took almost 100 years to fully discover. The combined results of many experiments were required in order to understand the pathway as a whole
4.
Metabolism
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Metabolism is the set of life-sustaining chemical transformations within the cells of living organisms. These enzyme-catalyzed reactions allow organisms to grow and reproduce, maintain their structures, usually, breaking down releases energy and building up consumes energy. The chemical reactions of metabolism are organized into metabolic pathways, in one chemical is transformed through a series of steps into another chemical. Enzymes act as catalysts that allow the reactions to proceed more rapidly, enzymes also allow the regulation of metabolic pathways in response to changes in the cells environment or to signals from other cells. The metabolic system of a particular organism determines which substances it will find nutritious, for example, some prokaryotes use hydrogen sulfide as a nutrient, yet this gas is poisonous to animals. The speed of metabolism, the rate, influences how much food an organism will require. A striking feature of metabolism is the similarity of the metabolic pathways. These striking similarities in metabolic pathways are likely due to their appearance in evolutionary history. Most of the structures that make up animals, plants and microbes are made from three classes of molecule, amino acids, carbohydrates and lipids. These biochemicals can be joined together to make such as DNA and proteins. Proteins are made of amino acids arranged in a linear chain joined together by peptide bonds, many proteins are enzymes that catalyze the chemical reactions in metabolism. Other proteins have structural or mechanical functions, such as those that form the cytoskeleton, Proteins are also important in cell signaling, immune responses, cell adhesion, active transport across membranes, and the cell cycle. Lipids are the most diverse group of biochemicals and their main structural uses are as part of biological membranes both internal and external, such as the cell membrane, or as a source of energy. Lipids are usually defined as hydrophobic or amphipathic biological molecules but will dissolve in organic solvents such as benzene or chloroform, the fats are a large group of compounds that contain fatty acids and glycerol, a glycerol molecule attached to three fatty acid esters is called a triacylglyceride. Several variations on this structure exist, including alternate backbones such as sphingosine in the sphingolipids. Steroids such as cholesterol are another class of lipids. Carbohydrates are aldehydes or ketones, with hydroxyl groups attached. Carbohydrates are the most abundant biological molecules, and fill numerous roles, such as the storage and transport of energy, the basic carbohydrate units are called monosaccharides and include galactose, fructose, and most importantly glucose
5.
Hexokinase
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A hexokinase is an enzyme that phosphorylates hexoses, forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, scientists have discovered and demonstrated that Hexokinase posses the ability to transfer a inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is an isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Genes that encode hexokinase have been discovered in every domain of life, and exist among a variety of species range from bacteria, yeast. They are categorized as actin fold proteins, sharing a common ATP binding site core that is surrounded by more variable sequences which determine substrate affinities, several hexokinase isoforms or isozymes that provide different functions can occur in a single species. Phosphorylation of a such as glucose often limits it to a number of intracellular metabolic processes. This is because phosphorylated hexoses are charged, and thus difficult to transport out of a cell. Most bacterial hexokinases are approximately 50 kD in size, multicellular organisms including plants and animals often have more than one hexokinase isoform. Most are about 100 kD in size and consist of two halves, which share much sequence homology and this suggests an evolutionary origin by duplication and fusion of a 50kD ancestral hexokinase similar to those of bacteria. There are four important mammalian hexokinase isozymes that vary in subcellular locations and kinetics with respect to different substrates and conditions, and physiological function. They are designated hexokinases I, II, III, and IV or hexokinases A, B, C, and D. Hexokinases I, II, Hexokinases I and II follow Michaelis-Menten kinetics at physiologic concentrations of substrates. All three are strongly inhibited by their product, glucose-6-phosphate, molecular weights are around 100 kD. Each consists of two similar 50kD halves, but only in hexokinase II do both halves have functional active sites, Hexokinase I/A is found in all mammalian tissues, and is considered a housekeeping enzyme, unaffected by most physiological, hormonal, and metabolic changes. Hexokinase II/B constitutes the principal regulated isoform in many types and is increased in many cancers. It is the hexokinase found in muscle and heart, Hexokinase II is also located at the mitochondria outer membrane so it can have direct access to ATP. Hexokinase III/C is substrate-inhibited by glucose at physiologic concentrations, little is known about the regulatory characteristics of this isoform. Mammalian hexokinase IV, also referred to as glucokinase, differs from other hexokinases in kinetics, the location of the phosphorylation on a subcellular level occurs when glucokinase translocates between the cytoplasm and nucleus of liver cells
6.
Carl Ferdinand Cori
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In 2004 both were designated a National Historic Chemical Landmark in recognition of their work that elucidated carbohydrate metabolism. Carl was the son of Carl Isidor Cori, a zoologist, and Maria née Lippich, the Cori Family came from the Papal State to the Royal Bohemian Crownland, Austrian Circle at the end of the 17th century. Carl Ferdinands grandfather Eduard Cori was an officer and beekeeper in Brüx. Carl Ferdinands younger sister Margarete Cori was a lecturer of Prague and he grew up in Trieste, where his father Carl Isidor was the director of the Marine Biological Station. In late 1914 the Cori family moved to Prague and Carl entered the school of Charles University in Prague. While studying there he met Gerty Theresa Radnitz and he was drafted into the Austro-Hungarian Army and served in the ski corps, and later was transferred to the sanitary corps, for which he set up a laboratory in Trieste. At the end of the war Carl completed his studies, graduating with Gerty in 1920, Carl and Gerty married that year and worked together in clinics in Vienna. Carl was invited to Graz to work with Otto Loewi to study the effect of the vagus nerve on the heart, while Carl was in Graz, Gerty remained in Vienna. A year later Carl was offered a position at the State Institute for the Study of Malignant Diseases in Buffalo, New York, in 1928, they became naturalized citizens of the United States. While at the Institute the Coris’ research focused on carbohydrate metabolism, in 1931 Carl accepted a position at the Washington University School of Medicine in St. Louis, Missouri. Carl joined as professor of pharmacology and in 1942 was made professor of biochemistry, in St. Louis, the Coris continued their research on glycogen and glucose and began to describe glycogenolysis, identifying and synthesizing the important enzyme glycogen phosphorylase. For these discoveries, they received the Nobel Prize in Physiology or Medicine in 1947, Gerty died in 1957 and Carl married Anne Fitz-Gerald Jones in 1960. He stayed on at Washington University until 1966, when he retired as chair of the biochemistry department and he was appointed visiting professor of Biological Chemistry at Harvard University while maintaining a laboratory space at the Massachusetts General Hospital, where he pursued research in genetics. From 1968 to 1983 he collaborated with noted geneticist Salomé Glüecksohn-Waelsch of the Albert Einstein College of Medicine in New York, in 1976 Carl received the Laurea honoris causa in Medicine from the University of Trieste. Cori was elected a Foreign Member of the Royal Society in 1950 and the Carl Cori Endowed Professorship at Washington University is named in his honor, currently held by Colin Nichols
7.
Myocyte
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Skeletal muscle is one of three major muscle types, the others being cardiac muscle and smooth muscle. It is a form of striated muscle tissue which is under the control of the somatic nervous system. Most skeletal muscles are attached to bones by bundles of collagen fibers known as tendons, a skeletal muscle refers to multiple bundles of cells called muscle fibers. The fibres and muscles are surrounded by connective tissue layers called fasciae, Muscle fibres, or muscle cells, are formed from the fusion of developmental myoblasts in a process known as myogenesis. Muscle fibres are cylindrical, and have more than one nucleus, Muscle fibers are in turn composed of myofibrils. The myofibrils are composed of actin and myosin filaments, repeated in units called sarcomeres, the sarcomere is responsible for the striated appearance of skeletal muscle, and forms the basic machinery necessary for muscle contraction. Connective tissue is present in all muscles as fascia, Muscle fibres are the individual contractile units within muscle. A single muscle such as the biceps contains many muscle fibres, another group of cells, the myosatellite cells are found between the basement membrane and the sarcolemma of muscle fibers. These cells are normally quiescent but can be activated by exercise or pathology to provide additional myonuclei for muscle growth or repair, development Individual muscle fibers are formed during development from the fusion of several undifferentiated immature cells known as myoblasts into long, cylindrical, multi-nucleated cells. Differentiation into this state is completed before birth with the cells continuing to grow in size thereafter. Microanatomy Skeletal muscle exhibits a distinctive banding pattern when viewed under the due to the arrangement of cytoskeletal elements in the cytoplasm of the muscle fibers. The principal cytoplasmic proteins are myosin and actin which are arranged in a unit called a sarcomere. The interaction of myosin and actin is responsible for muscle contraction, every single organelle and macromolecule of a muscle fiber is arranged to ensure form meets function. The cell membrane is called the sarcolemma with the known as the sarcoplasm. In the sarcoplasm are the myofibrils, the myofibrils are long protein bundles about 1 micrometer in diameter each containing myofilaments. Pressed against the inside of the sarcolemma are the unusual flattened myonuclei, between the myofibrils are the mitochondria. While the muscle fiber does not have a smooth endoplasmic reticulum, the sarcoplasmic reticulum surrounds the myofibrils and holds a reserve of the calcium ions needed to cause a muscle contraction. Periodically, it has dilated end sacs known as terminal cisternae and these cross the muscle fiber from one side to the other
8.
Skeletal muscle
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Skeletal muscle is one of three major muscle types, the others being cardiac muscle and smooth muscle. It is a form of striated muscle tissue which is under the control of the somatic nervous system. Most skeletal muscles are attached to bones by bundles of collagen fibers known as tendons, a skeletal muscle refers to multiple bundles of cells called muscle fibers. The fibres and muscles are surrounded by connective tissue layers called fasciae, Muscle fibres, or muscle cells, are formed from the fusion of developmental myoblasts in a process known as myogenesis. Muscle fibres are cylindrical, and have more than one nucleus, Muscle fibers are in turn composed of myofibrils. The myofibrils are composed of actin and myosin filaments, repeated in units called sarcomeres, the sarcomere is responsible for the striated appearance of skeletal muscle, and forms the basic machinery necessary for muscle contraction. Connective tissue is present in all muscles as fascia, Muscle fibres are the individual contractile units within muscle. A single muscle such as the biceps contains many muscle fibres, another group of cells, the myosatellite cells are found between the basement membrane and the sarcolemma of muscle fibers. These cells are normally quiescent but can be activated by exercise or pathology to provide additional myonuclei for muscle growth or repair, development Individual muscle fibers are formed during development from the fusion of several undifferentiated immature cells known as myoblasts into long, cylindrical, multi-nucleated cells. Differentiation into this state is completed before birth with the cells continuing to grow in size thereafter. Microanatomy Skeletal muscle exhibits a distinctive banding pattern when viewed under the due to the arrangement of cytoskeletal elements in the cytoplasm of the muscle fibers. The principal cytoplasmic proteins are myosin and actin which are arranged in a unit called a sarcomere. The interaction of myosin and actin is responsible for muscle contraction, every single organelle and macromolecule of a muscle fiber is arranged to ensure form meets function. The cell membrane is called the sarcolemma with the known as the sarcoplasm. In the sarcoplasm are the myofibrils, the myofibrils are long protein bundles about 1 micrometer in diameter each containing myofilaments. Pressed against the inside of the sarcolemma are the unusual flattened myonuclei, between the myofibrils are the mitochondria. While the muscle fiber does not have a smooth endoplasmic reticulum, the sarcoplasmic reticulum surrounds the myofibrils and holds a reserve of the calcium ions needed to cause a muscle contraction. Periodically, it has dilated end sacs known as terminal cisternae and these cross the muscle fiber from one side to the other
9.
Fermentation
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Fermentation is a metabolic process that converts sugar to acids, gases, or alcohol. It occurs in yeast and bacteria, and also in oxygen-starved muscle cells, Fermentation is also used more broadly to refer to the bulk growth of microorganisms on a growth medium, often with the goal of producing a specific chemical product. French microbiologist Louis Pasteur is often remembered for his insights into fermentation, the science of fermentation is known as zymology. Fermentation takes place when the transport chain is unusable. In this case it becomes the primary means of ATP production. Fermentation turns NADH and pyruvate produced in glycolysis into NAD+. In the presence of O2, NADH and pyruvate are used to generate ATP in respiration and this is called oxidative phosphorylation, and it generates much more ATP than glycolysis alone. For that reason, cells generally benefit from avoiding fermentation when oxygen is available, the exception being obligate anaerobes which cannot tolerate oxygen. The first step, glycolysis, is common to all fermentation pathways, two ADP molecules and two Pi are converted to two ATP and two water molecules via substrate-level phosphorylation. Two molecules of NAD+ are also reduced to NADH, in oxidative phosphorylation the energy for ATP formation is derived from an electrochemical proton gradient generated across the inner mitochondrial membrane via the electron transport chain. Humans have used fermentation to produce drinks and beverages since the Neolithic age, Fermentation can even occur within the stomachs of animals, such as humans. To many people, fermentation simply means the production of alcohol, grains and fruits are fermented to produce beer, if a food soured, one might say it was off or fermented. Here are some definitions of fermentation and they range from informal, general usage to more scientific definitions. Preservation methods for food via microorganisms, any process that produces alcoholic beverages or acidic dairy products. Any large-scale microbial process occurring with or without air, any energy-releasing metabolic process that takes place only under anaerobic conditions. Fermentation does not necessarily have to be carried out in an anaerobic environment, for example, even in the presence of abundant oxygen, yeast cells greatly prefer fermentation to aerobic respiration, as long as sugars are readily available for consumption. The antibiotic activity of hops also inhibits aerobic metabolism in yeast, Fermentation reacts NADH with an endogenous, organic electron acceptor. Usually this is formed from the sugar during the glycolysis step. Sugars are the most common substrate of fermentation, and typical examples of products are ethanol, lactic acid, carbon dioxide
10.
Fasting
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Fasting is a willing abstinence or reduction from some or all food, drink, or both, for a period of time. An absolute fast is normally defined as abstinence from all food and liquid for a period, usually a period of 24 hours. Water fasting allows drinking water but nothing else, other fasts may be partially restrictive, limiting only particular foods or substances. A fast may also be intermittent in nature, Fasting practices may preclude intercourse and other activities as well as food. In a physiological context, fasting may refer to the status of a person who has not eaten overnight. Several metabolic adjustments occur during fasting, and some tests are used to determine a fasting state. For example, a person is assumed to be fasting after 8–12 hours from their last meal, metabolic changes toward the fasting state begin after absorption of a meal, post-absorptive state is synonymous with this usage, in contrast to the postprandial state of ongoing digestion. A diagnostic fast refers to prolonged fasting conducted under observation for investigation of a problem, many people may also fast as part of a medical procedure or check-up such as a colonoscopy. Fasting is also a part of religious observances. Fasting is often practiced prior to surgery or other procedures that require general anesthetics because of the risk of aspiration of gastric contents after induction of anesthesia. Additionally, certain tests, such as cholesterol testing or certain blood glucose measurements require fasting for several hours so that a baseline can be established. In the case of a panel, failure to fast for a full 12 hours will guarantee an elevated triglyceride measurement. Fasting is of no help in preventing or treating cancer. Fasting can help alleviate symptoms of depression. However the psychological effects may include anxiety and depression. Fasting will lead to weight loss, using fasting for weight loss is considered dangerous. It has been argued that fasting makes one better appreciate food, Fasting is often used as a tool to make a political statement, to protest, or to bring awareness to a cause. A hunger strike is a method of non-violent resistance in which participants fast as an act of political protest, or to provoke feelings of guilt, a spiritual fast incorporates personal spiritual beliefs with the desire to express personal principles, sometimes in the context of a social injustice
11.
Glycogen
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Glycogen is a multibranched polysaccharide of glucose that serves as a form of energy storage in humans, animals, and fungi. The polysaccharide structure represents the main form of glucose in the body. In humans, glycogen is made and stored primarily in the cells of the liver, glycogen functions as the secondary long-term energy storage, with the primary energy stores being fats held in adipose tissue. Muscle glycogen is converted into glucose by muscle cells, and liver glycogen converts to glucose for use throughout the body including the nervous system. Glycogen is the analogue of starch, a polymer that functions as energy storage in plants. It has a similar to amylopectin, but is more extensively branched. Both are white powders in their dry state, glycogen is found in the form of granules in the cytosol/cytoplasm in many cell types, and plays an important role in the glucose cycle. Glycogen forms a reserve that can be quickly mobilized to meet a sudden need for glucose. In the liver, glycogen can make up from 5–6% of the fresh weight. Only the glycogen stored in the liver can be accessible to other organs. In the muscles, glycogen is found in a low concentration, the amount of glycogen stored in the body—especially within the muscles, liver, and red blood cells—mostly depends on physical training, basal metabolic rate, and eating habits. Small amounts of glycogen are found in the kidneys, and even smaller amounts in certain cells in the brain. The uterus also stores glycogen during pregnancy to nourish the embryo, glycogen is a branched biopolymer consisting of linear chains of glucose residues with further chains branching off every 8 to 12 glucoses or so. Glucoses are linked together linearly by α glycosidic bonds from one glucose to the next, branches are linked to the chains from which they are branching off by α glycosidic bonds between the first glucose of the new branch and a glucose on the stem chain. Due to the way glycogen is synthesised, every glycogen granule has at its core a glycogenin protein. Glycogen in muscle, liver, and fat cells is stored in a hydrated form, as a meal containing carbohydrates or protein is eaten and digested, blood glucose levels rise, and the pancreas secretes insulin. Blood glucose from the vein enters liver cells. Insulin acts on the hepatocytes to stimulate the action of several enzymes, glucose molecules are added to the chains of glycogen as long as both insulin and glucose remain plentiful
12.
Nicotinamide adenine dinucleotide
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Nicotinamide adenine dinucleotide is a coenzyme found in all living cells. The compound is a dinucleotide, because it consists of two nucleotides joined through their phosphate groups, one nucleotide contains an adenine base and the other nicotinamide. Nicotinamide adenine dinucleotide exists in two forms, an oxidized and reduced form abbreviated as NAD+ and NADH respectively, in metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The coenzyme is, therefore, found in two forms in cells, NAD+ is an oxidizing agent – it accepts electrons from other molecules and becomes reduced and this reaction forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the function of NAD. However, it is used in other cellular processes, the most notable one being a substrate of enzymes that add or remove chemical groups from proteins. Because of the importance of these functions, the involved in NAD metabolism are targets for drug discovery. In organisms, NAD can be synthesized from simple building-blocks from the amino acids tryptophan or aspartic acid, in an alternative fashion, more complex components of the coenzymes are taken up from food as the vitamin called niacin. Similar compounds are released by reactions that break down the structure of NAD and these preformed components then pass through a salvage pathway that recycles them back into the active form. Some NAD is also converted into nicotinamide adenine dinucleotide phosphate, the chemistry of this related coenzyme is similar to that of NAD, nicotinamide adenine dinucleotide, like all dinucleotides, consists of two nucleosides joined by a pair of bridging phosphate groups. The nucleosides each contain a ring, one with adenine attached to the first carbon atom. The nicotinamide moiety can be attached in two orientations to this carbon atom. Because of these two structures, the compound exists as two diastereomers. It is the diastereomer of NAD+ that is found in organisms. These nucleotides are joined together by a bridge of two groups through the 5 carbons. In metabolism, the compound accepts or donates electrons in redox reactions, such reactions involve the removal of two hydrogen atoms from the reactant, in the form of a hydride ion, and a proton. The proton is released into solution, while the reductant RH2 is oxidized, the midpoint potential of the NAD+/NADH redox pair is −0.32 volts, which makes NADH a strong reducing agent. The reaction is reversible, when NADH reduces another molecule and is re-oxidized to NAD+
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